ID K2FP24_9BACI Unreviewed; 364 AA.
AC K2FP24;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE RecName: Full=Prephenate dehydrogenase {ECO:0000256|ARBA:ARBA00016891};
DE EC=1.3.1.12 {ECO:0000256|ARBA:ARBA00012068};
GN ORFNames=MJ3_01572 {ECO:0000313|EMBL:EKE32606.1};
OS Salimicrobium jeotgali.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Salimicrobium.
OX NCBI_TaxID=1230341 {ECO:0000313|EMBL:EKE32606.1, ECO:0000313|Proteomes:UP000011746};
RN [1] {ECO:0000313|EMBL:EKE32606.1, ECO:0000313|Proteomes:UP000011746}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MJ3 {ECO:0000313|EMBL:EKE32606.1,
RC ECO:0000313|Proteomes:UP000011746};
RX PubMed=23144427; DOI=10.1128/JB.01808-12;
RA Lee S.H., Jung J.Y., Jeon C.O.;
RT "Draft Genome Sequence of Salimicrobium sp. Strain MJ3, Isolated from
RT Myulchi-Jeot, Korean Fermented Seafood.";
RL J. Bacteriol. 194:6695-6695(2012).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NAD(+) + prephenate = 3-(4-hydroxyphenyl)pyruvate + CO2 +
CC NADH; Xref=Rhea:RHEA:13869, ChEBI:CHEBI:16526, ChEBI:CHEBI:29934,
CC ChEBI:CHEBI:36242, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.3.1.12;
CC Evidence={ECO:0000256|ARBA:ARBA00001162};
CC -!- PATHWAY: Amino-acid biosynthesis; L-tyrosine biosynthesis; (4-
CC hydroxyphenyl)pyruvate from prephenate (NAD(+) route): step 1/1.
CC {ECO:0000256|ARBA:ARBA00005067}.
CC -!- SIMILARITY: Belongs to the prephenate/arogenate dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00007964}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EKE32606.1}.
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DR EMBL; AMPQ01000002; EKE32606.1; -; Genomic_DNA.
DR RefSeq; WP_008587510.1; NZ_JAFBFF010000002.1.
DR AlphaFoldDB; K2FP24; -.
DR STRING; 1230341.AAV35_006155; -.
DR KEGG; sje:AAV35_006155; -.
DR PATRIC; fig|1230341.3.peg.331; -.
DR eggNOG; COG0287; Bacteria.
DR OrthoDB; 9802008at2; -.
DR UniPathway; UPA00122; UER00961.
DR Proteomes; UP000011746; Unassembled WGS sequence.
DR GO; GO:0070403; F:NAD+ binding; IEA:InterPro.
DR GO; GO:0008977; F:prephenate dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR GO; GO:0004665; F:prephenate dehydrogenase (NADP+) activity; IEA:InterPro.
DR GO; GO:0006571; P:tyrosine biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd04909; ACT_PDH-BS; 1.
DR Gene3D; 3.30.70.260; -; 1.
DR Gene3D; 1.10.3660.10; 6-phosphogluconate dehydrogenase C-terminal like domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR045865; ACT-like_dom_sf.
DR InterPro; IPR002912; ACT_dom.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR046825; PDH_C.
DR InterPro; IPR046826; PDH_N.
DR InterPro; IPR003099; Prephen_DH.
DR PANTHER; PTHR21363; PREPHENATE DEHYDROGENASE; 1.
DR PANTHER; PTHR21363:SF0; PREPHENATE DEHYDROGENASE [NADP(+)]; 1.
DR Pfam; PF01842; ACT; 1.
DR Pfam; PF20463; PDH_C; 1.
DR Pfam; PF02153; PDH_N; 1.
DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF55021; ACT-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS51671; ACT; 1.
DR PROSITE; PS51176; PDH_ADH; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00023141};
KW Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:EKE32606.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000011746};
KW Tyrosine biosynthesis {ECO:0000256|ARBA:ARBA00022498}.
FT DOMAIN 3..289
FT /note="Prephenate/arogenate dehydrogenase"
FT /evidence="ECO:0000259|PROSITE:PS51176"
FT DOMAIN 294..364
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 364 AA; 41039 MW; 8534F413B6A3C45B CRC64;
MNKTVVVAGL GLIGGSLAMN IKKEGHFILG HDEDVQSLEL AYRQGVIDEK AEDLYEALSR
ADVLFLALPI TTTVQVIRKL NNVTLTKDLL VTDVSSVKNE VMKEASLLTN DRITFIGGHP
MSGSHKNGFT AAKPHLFENA IYVLSPVNDR DEKTKELREL LEATKARFVT LSPQEHDEMT
AVISHFPHLI ASSLVQQAKK WQHTHPELKN LAAGGFRDIT RIASSNPPLW QDIFFQNKQQ
LVPMLEDWIQ EMTRLKEYLQ NDSQEETLRY LTEAKTFRDG LPVKEKGAIP GFYDIFVDIY
DQPGTIHKVI EVLAEAGISI KNIEILEIRE GITGVLRISF PTGKEQEESA LLLRRKNYEV
VIEQ
//
